ArticleGenes & development2003
An intersubunit contact stimulating transcription initiation by E coli RNA polymerase: interaction of the alpha C-terminal domain and sigma region 4.
Article in Genes & development, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
48 citing papers in PubMed, 82 citations in OpenAlex.
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- Structural basis of dual activation of cell division by the actinobacterial transcription factors WhiA and WhiB.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Some novel features of strong promoters discovered in Cytophaga hutchinsonii.Applied microbiology and biotechnology · 2022Article
- Distinct Interaction Mechanism of RNA Polymerase and ResD at Proximal and Distal Subsites for Transcription Activation of Nitrite Reductase in Bacillus subtilis.Journal of bacteriology · 2022Article
- Structural origins ofProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Activation by TyrR in Escherichia coli K-12 by Interaction between TyrR and the α-Subunit of RNA Polymerase.Journal of bacteriology · 2021Article
- The Context-Dependent Influence of Promoter Sequence Motifs on Transcription Initiation Kinetics and Regulation.Journal of bacteriology · 2021Review
- Structural Basis for Virulence Activation of Francisella tularensis.Molecular cell · 2021Article
- The RNA Polymerase α Subunit Recognizes the DNA Shape of the Upstream Promoter Element.Biochemistry · 2020Article
- Activation by NarL at the Escherichia coli ogt promoter.The Biochemical journal · 2020Article
- Stepwise Promoter Melting by Bacterial RNA Polymerase.Molecular cell · 2020Article
- Structural basis of non-canonical transcriptional regulation by the σA-bound iron-sulfur protein WhiB1 in M. tuberculosis.Nucleic acids research · 2020Article
- EnvZ/OmpR Two-Component Signaling: An Archetype System That Can Function Noncanonically.EcoSal Plus · 2020Review
- Article
- T7 phage factor required for managing RpoS inProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Exploring the Amino Acid Residue Requirements of the RNA Polymerase (RNAP) α Subunit C-Terminal Domain for Productive Interaction between Spx and RNAP of Bacillus subtilis.Journal of bacteriology · 2017Article
- Structural insights into the mycobacteria transcription initiation complex from analysis of X-ray crystal structures.Nature communications · 2017Article
- Fluorescence Resonance Energy Transfer Characterization of DNA Wrapping in Closed and Open Escherichia coli RNA Polymerase-λP(R) Promoter Complexes.Biochemistry · 2016Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The C-terminal domain of the Escherichia coli RNA polymerase (RNAP) alpha subunit (alphaCTD) stimulates transcription initiation by interacting with upstream (UP) element DNA and a variety of transcription activators. Here we identify specific substitutions in region 4.2 of sigma 70 (sigma(70)) and in alphaCTD that decrease transcription initiation from promoters containing some, but not all, UP elements. This decrease in transcription derives from a decrease in the initial equilibrium constant for RNAP binding (K(B)). The open complexes formed by the mutant and wild-type RNAPs differ in DNAse I sensitivity at the junction of the alphaCTD and sigma DNA binding sites, correlating with the differences in transcription. A model of the DNA-alphaCTD-sigma region 4.2 ternary complex, constructed from the previously determined X-ray structures of the Thermus aquaticus sigma region 4.2-DNA complex and the E. coli alphaCTD-DNA complex, indicates that the residues identified by mutation in sigma region 4.2 and in alphaCTD are in very close proximity. Our results strongly suggest that alphaCTD, when bound to an UP element proximal subsite, contacts the RNAP sigma(70) subunit, increasing transcription. Previous data from the literature suggest that this same sigma-alphaCTD interaction also plays a role in transcription factor-mediated activation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.